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Aguilar, R.C.; Longhi, S.A.; Shaw, J.D.; Yeh, L.-Y.; Kim, S.; Schön, A.; Freire, E.; Hsu, A.; McCormick, W.K.; Watson, H.A.; Wendland, B. "Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins" (2006) Proceedings of the National Academy of Sciences of the United States of America. 103(11):4116-4121
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Abstract:

Epsins are endocytic proteins with a structured epsin N-terminal homology (ENTH) domain that binds phosphoinositides and a poorly structured C-terminal region that interacts with ubiquitin and endocytic machinery, including clathrin and endocytic scaffolding proteins. Yeast has two redundant genes encoding epsins, ENT1 and ENT2; deleting both genes is lethal. We demonstrate that the ENTH domain is both necessary and sufficient for viability of ent1Δent2Δ cells. Mutational analysis of the ENTH domain revealed a surface patch that is essential for viability and that binds guanine nucleotide triphosphatase-activating proteins for Cdc42, a critical regulator of cell polarity in all eukaryotes. Furthermore, the epsins contribute to regulation of specific Cdc42 signaling pathways in yeast cells. These data support a model in which the epsins function as spatial and temporal coordinators of endocytosis and cell polarity. © 2006 by The National Academy of Sciences of the USA.

Registro:

Documento: Artículo
Título:Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins
Autor:Aguilar, R.C.; Longhi, S.A.; Shaw, J.D.; Yeh, L.-Y.; Kim, S.; Schön, A.; Freire, E.; Hsu, A.; McCormick, W.K.; Watson, H.A.; Wendland, B.
Filiación:Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, United States
Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-2054, United States
Instituto de Investigaciones en Ingenieria Genetica y Biologia Molecular (INGEBI-CONICET), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, 1428 Buenos Aires, Argentina
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, United States
Palabras clave:Actin; Endocytosis; Polarity; clathrin; epsin; guanosine triphosphatase activating protein; phosphatidylinositide; protein Cdc42; scaffold protein; amino terminal sequence; article; cell polarity; endocytosis; ENT1 gene; ENT2 gene; fungal gene; nonhuman; priority journal; protein domain; protein protein interaction; sequence homology; yeast; Adaptor Proteins, Signal Transducing; Carrier Proteins; cdc42 GTP-Binding Protein, Saccharomyces cerevisiae; Cell Polarity; Endocytosis; Genes, Fungal; Models, Molecular; Mutation; Phenotype; Protein Structure, Tertiary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Eukaryota
Año:2006
Volumen:103
Número:11
Página de inicio:4116
Página de fin:4121
DOI: http://dx.doi.org/10.1073/pnas.0510513103
Título revista:Proceedings of the National Academy of Sciences of the United States of America
Título revista abreviado:Proc. Natl. Acad. Sci. U. S. A.
ISSN:00278424
CODEN:PNASA
CAS:Adaptor Proteins, Signal Transducing; Carrier Proteins; cdc42 GTP-Binding Protein, Saccharomyces cerevisiae, EC 3.6.5.2; ENT1 protein, S cerevisiae; ENT2 protein, S cerevisiae; Saccharomyces cerevisiae Proteins
PDF:https://bibliotecadigital.exactas.uba.ar/download/paper/paper_00278424_v103_n11_p4116_Aguilar.pdf
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00278424_v103_n11_p4116_Aguilar

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Citas:

---------- APA ----------
Aguilar, R.C., Longhi, S.A., Shaw, J.D., Yeh, L.-Y., Kim, S., Schön, A., Freire, E.,..., Wendland, B. (2006) . Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins. Proceedings of the National Academy of Sciences of the United States of America, 103(11), 4116-4121.
http://dx.doi.org/10.1073/pnas.0510513103
---------- CHICAGO ----------
Aguilar, R.C., Longhi, S.A., Shaw, J.D., Yeh, L.-Y., Kim, S., Schön, A., et al. "Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins" . Proceedings of the National Academy of Sciences of the United States of America 103, no. 11 (2006) : 4116-4121.
http://dx.doi.org/10.1073/pnas.0510513103
---------- MLA ----------
Aguilar, R.C., Longhi, S.A., Shaw, J.D., Yeh, L.-Y., Kim, S., Schön, A., et al. "Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins" . Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 11, 2006, pp. 4116-4121.
http://dx.doi.org/10.1073/pnas.0510513103
---------- VANCOUVER ----------
Aguilar, R.C., Longhi, S.A., Shaw, J.D., Yeh, L.-Y., Kim, S., Schön, A., et al. Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins. Proc. Natl. Acad. Sci. U. S. A. 2006;103(11):4116-4121.
http://dx.doi.org/10.1073/pnas.0510513103